CPLM-002761

Genbank Nucleotide ID

U1 small nuclear ribonucleoprotein C

Protein Synonyms/Alias

U1 snRNP C; U1-C; U1C

Homo sapiens (Human)

Position	Peptide	Type	References
3	*****MPKFYCDYCD	ubiquitination	[1, 2, 3, 4, 5, 6]
40	NVKDYYQKWMEEQAQ	ubiquitination	[1, 5]
52	QAQSLIDKTTAAFQQ	acetylation	[7, 8]
52	QAQSLIDKTTAAFQQ	ubiquitination	[4, 9]

[1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[9] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]

Functional Description

Component of the U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates E complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region.

ZN_FING 4 36 Matrin-type.
MOD_RES 8 8 Phosphotyrosine.
MOD_RES 17 17 Phosphoserine.
MOD_RES 52 52 N6-acetyllysine.

3D-structure; Acetylation; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein; RNA-binding; Zinc; Zinc-finger.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0015030; C:Cajal body; IDA:UniProtKB.
GO:0000243; C:commitment complex; IEA:HAMAP.
GO:0005685; C:U1 snRNP; IDA:UniProtKB.
GO:0071004; C:U2-type prespliceosome; IEA:HAMAP.
GO:0003729; F:mRNA binding; IEA:HAMAP.
GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO:0000395; P:mRNA 5'-splice site recognition; IEA:HAMAP.
GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.

IPR017340; U1_snRNP-C.
IPR000690; Znf_C2H2_matrin.
IPR003604; Znf_U1.
IPR013085; Znf_U1-C.